Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808  1390 FRALETEGLLLYNGNAHGKDFLALALLDGHVQFRFDTGSGPAVLTSSVPVEPGRWHRLELSRHWRQGTLSVDGEIPVVGE 1469
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 537231808  1470 SPSGTDG-LNLDTNLFVGGIPEEqaAMVLDRTSVGSGLKGCIRMLDINNQQLD 1521
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808  1889 RTEATQGLVLWSGKATERaDYVALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREQREGSLQVGNEAPVTGS 1968
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 537231808  1969 SPLGATQ-LDTDGALWLGGLQKLPVgQTLPKAYGTGFVGCLRDVVVGHRHLH 2019
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808   1130 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDAKKDFWSVHLRDLGPGKLVRAVVDVHFD 1209
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 537231808   1210 PATTfqASDVGRALLRQIQVSRpWALAVRRplQEHVRFLDFDWFPT 1255
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQAA-YSLKITN--VNVVDVLDPDSADS 121

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 537231808    556 VCPTECVASARPVCGSDGRTYASECELHVHACTHQISLHVASAGHC 601
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 537231808    198 VCKKNvCPATVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 537231808    706 VCDFSCQSVLRsPVCGSDGITYNTECDLKKARCESQQELYVAAQGAC 752
Cdd:smart00280    1 DCPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 537231808    924 VCPTlTCPEaNSTKVCGSDGVTYGNECQLKTIACRQGLDISTQSLGPC 971
Cdd:smart00280    1 DCPE-ACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 537231808  423 CDGTYRPVCAQDGHTYDNDCWRQQAECRQQHAIPPKHQGPC 463
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 537231808 1812 ASGNPCLNGGSCVPREATYECLCPGGFSGLHCE 1844
Cdd:cd00054     6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808  1390 FRALETEGLLLYNGNAHGKDFLALALLDGHVQFRFDTGSGPAVLTSSVPVEPGRWHRLELSRHWRQGTLSVDGEIPVVGE 1469
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 537231808  1470 SPSGTDG-LNLDTNLFVGGIPEEqaAMVLDRTSVGSGLKGCIRMLDINNQQLD 1521
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808 1367 FEGHSFLAFPTLRA-YHTLRLALEFRALETEGLLLYNGNAHGKDFLALALLDGHVQFRFDTGSGPAVLTSSVPVEPGRWH 1445
Cdd:cd00110     4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 537231808 1446 RLELSRHWRQGTLSVDGEIPVVGESPSGTDGLNLDTNLFVGGIPEEQAamvLDRTSVGSGLKGCIRMLDIN 1516
Cdd:cd00110    84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLK---SPGLPVSPGFVGCIRDLKVN 151

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808  1659 FLARGASGLLLYNGQKTDGkgDFVSLALHNQHLEFRYDLGKGAAVIRSKEPIALGTWIRVSLERNGRKGALRVGDGPRVL 1738
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 537231808  1739 GESPV-PHTMLNLKEPLYVGGAPDFSKLARGAAVSSGFDGAIQLVSLSGYQLL 1790
Cdd:pfam00054   79 GESPLgATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808 1631 FSGFSYLELKGLHTFERDlgekMALEMVFLARGASGLLLYNGQKTdgKGDFVSLALHNQHLEFRYDLGKGAAVIRSKEPI 1710
Cdd:cd00110     4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537231808 1711 ALGTWIRVSLERNGRKGALRVGDGPRVLGESPVPHTMLNLKEPLYVGGAPDFSKLaRGAAVSSGFDGAIQLVSL 1784
Cdd:cd00110    78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150

Laminin G domain;

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808   1655 LEMVFLARGASGLLLYNGQKtdGKGDFVSLALHNQHLEFRYDLGKGAAVIRSK-EPIALGTWIRVSLERNGRKGALRVGD 1733
Cdd:smart00282    2 ISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 537231808   1734 GPRVLGESPVPHTMLNLKEPLYVGGAPDFSKLARGaAVSSGFDGAIQLVSLSG 1786
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNG 131

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808   1130 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDAKKDFWSVHLRDLGPGKLVRAVVDVHFD 1209
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 537231808   1210 PATTfqASDVGRALLRQIQVSRpWALAVRRplQEHVRFLDFDWFPT 1255
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQAA-YSLKITN--VNVVDVLDPDSADS 121

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 537231808  795 CHCNPHGSYSGTCDPATGQCSCRPGVGGLRCDRCEPGFWNF 835
Cdd:cd00055     2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 537231808    556 VCPTECVASARPVCGSDGRTYASECELHVHACTHQISLHVASAGHC 601
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 537231808    198 VCKKNvCPATVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 537231808    274 CPTTCFGATDgPVCGSDGIDYPSECQLLRHACDHQEHVFKKFDGPC 319
Cdd:smart00280    2 CPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 537231808  557 CPTECvasaRPVCGSDGRTYASECELHVHACTHQISLHVASAGHC 601
Cdd:cd00104     1 CPKEY----DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 537231808    621 VCPRCEHPPPGPVCGSDGVTYTSACELREAACQQQVEIEEARAGPC 666
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 537231808    924 VCPTlTCPEaNSTKVCGSDGVTYGNECQLKTIACRQGLDISTQSLGPC 971
Cdd:smart00280    1 DCPE-ACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 537231808  622 CPRCEHPppgpVCGSDGVTYTSACELREAACQQQVEIEEARAGPC 666
Cdd:cd00104     1 CPKEYDP----VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 537231808   351 CPAKHAPVCGDDGVTYENDCVMGRIGATRGLLLQKVRSGQC 391
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 537231808  930 CPEaNSTKVCGSDGVTYGNECQLKTIACRQGLDISTQSLGPC 971
Cdd:cd00104     1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 537231808  285 PVCGSDGIDYPSECQLLRHACDHQEHVFKKFDGPC 319
Cdd:cd00104     7 PVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Laminin-type epidermal growth factor-like domai;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 537231808    849 CSCDPRGAVRDDCEQMTGLCSCRPGVSGPKCGQCPDG 885
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 537231808  351 CPAKHAPVCGDDGVTYENDCVMGRIGATRGLLLQKVRSGQC 391
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 537231808   620 CVCPRCEHPPPGPVCGSDGVTYTSACELREAACQQQVEIEEARA---GPC 666
Cdd:pfam07648    1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKVkydGSC 50

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 537231808   707 CDFSCQSVLRSPVCGSDGITYNTECDLKKARCESQQEL 744
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....
gi 537231808   1812 ASGNPCLNGGSCVPREATYECLCPGGFS-GLHCE 1844
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 537231808   496 CSGIYDPVCGTDDVTYGSVCELesmaCALKRE----IRVARKGPC 536
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLF----CAENGKrgtnLHKVHDGEC 49

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 537231808   416 CSCDRVicdgTYRPVCAQDGHTYDNDCWRQQAECRQQ---HAIPPKHQGPC 463
Cdd:pfam07648    4 CQCPKT----EYEPVCGSDGVTYPSPCALCAAGCKLGkevKEEKVKYDGSC 50

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.

                           10        20        30
                   ....*....|....*....|....*....|.
gi 537231808  1323 CDSQPCLHGGTCqdQDSGKGFTCICTAGRGG 1353
Cdd:pfam00008    1 CAPNPCSNGGTC--VDTPGGYTCICPEGYTG 29

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808  1390 FRALETEGLLLYNGNAHGKDFLALALLDGHVQFRFDTGSGPAVLTSSVPVEPGRWHRLELSRHWRQGTLSVDGEIPVVGE 1469
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 537231808  1470 SPSGTDG-LNLDTNLFVGGIPEEqaAMVLDRTSVGSGLKGCIRMLDINNQQLD 1521
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808 1367 FEGHSFLAFPTLRA-YHTLRLALEFRALETEGLLLYNGNAHGKDFLALALLDGHVQFRFDTGSGPAVLTSSVPVEPGRWH 1445
Cdd:cd00110     4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 537231808 1446 RLELSRHWRQGTLSVDGEIPVVGESPSGTDGLNLDTNLFVGGIPEEQAamvLDRTSVGSGLKGCIRMLDIN 1516
Cdd:cd00110    84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLK---SPGLPVSPGFVGCIRDLKVN 151

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808  1659 FLARGASGLLLYNGQKTDGkgDFVSLALHNQHLEFRYDLGKGAAVIRSKEPIALGTWIRVSLERNGRKGALRVGDGPRVL 1738
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 537231808  1739 GESPV-PHTMLNLKEPLYVGGAPDFSKLARGAAVSSGFDGAIQLVSLSGYQLL 1790
Cdd:pfam00054   79 GESPLgATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537231808 1631 FSGFSYLELKGLHTFERDlgekMALEMVFLARGASGLLLYNGQKTdgKGDFVSLALHNQHLEFRYDLGKGAAVIRSKEPI 1710
Cdd:cd00110     4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537231808 1711 ALGTWIRVSLERNGRKGALRVGDGPRVLGESPVPHTMLNLKEPLYVGGAPDFSKLaRGAAVSSGFDGAIQLVSL 1784
Cdd:cd00110    78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150